001     94235
005     20250731122618.0
024 7 _ |a pmid:19940249
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024 7 _ |a pmc:PMC2795549
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024 7 _ |a 1091-6490
|2 ISSN
024 7 _ |a 0027-8424
|2 ISSN
024 7 _ |a 10.1073/pnas.0911789106
|2 doi
024 7 _ |a WOS:000272795300022
|2 WOS
024 7 _ |a altmetric:20934385
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024 7 _ |a openalex:W2166335706
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037 _ _ |a PHPPUBDB-12319
041 _ _ |a eng
082 _ _ |a 000
100 1 _ |a Cao, X.
110 1 _ |a DESY
|b European Molecular Biology Laboratory
245 _ _ |a Golgi protein FAPP2 tubulates membranes
260 _ _ |a Washington, DC
|c 2009
|b Academy
300 _ _ |a 21121-21125
336 7 _ |a Journal Article
|0 0
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336 7 _ |a article
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336 7 _ |a Journal Article
|b journal
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336 7 _ |a ARTICLE
|2 BibTeX
440 _ 0 |a Proc. Nat. Acad. Sci. USA
|0 PERI:(DE-600)1461794-8
|v 106
|x 1091-6490
500 _ _ |3 Converted on 2013-05-30 14:57
500 _ _ |3 Converted on 2013-06-21 19:21
520 _ _ |a The Golgi-associated four-phosphate adaptor protein 2 (FAPP2) has been shown to possess transfer activity for glucosylceramide both in vitro and in cells. We have previously shown that FAPP2 is involved in apical transport from the Golgi complex in epithelial MDCK cells. In this paper we assign an unknown activity for the protein as well as providing structural insight into protein assembly and a low-resolution envelope structure. By applying analytical ultracentrifugation and small-angle x-ray scattering, we show that FAPP2 is a dimeric protein in solution, having a curved shape 30 nm in length. The purified FAPP2 protein has the capability to form tubules from membrane sheets in vitro. This activity is dependent on the phosphoinositide-binding activity of the PH domain of FAPP2. These data suggest that FAPP2 functions directly in the formation of apical carriers in the trans-Golgi network.
536 _ _ |0 G:(DE-H253)POF1-No-Ref-20130405
|f POF I
|x 0
|c POF1-550
|a FS Beamline without reference (POF1-550)
588 _ _ |a Dataset connected to Pubmed
650 _ 7 |a Adaptor Proteins, Signal Transducing
|0 0
|2 NLM Chemicals
650 _ 7 |a Lipid Bilayers
|0 0
|2 NLM Chemicals
650 _ 7 |a PLEKHA8 protein, human
|0 0
|2 NLM Chemicals
650 _ 7 |a Phosphatidylinositols
|0 0
|2 NLM Chemicals
650 _ 7 |a Solutions
|0 0
|2 NLM Chemicals
650 _ 2 |a Adaptor Proteins, Signal Transducing: chemistry
|2 MeSH
650 _ 2 |a Adaptor Proteins, Signal Transducing: metabolism
|2 MeSH
650 _ 2 |a Adaptor Proteins, Signal Transducing: physiology
|2 MeSH
650 _ 2 |a Animals
|2 MeSH
650 _ 2 |a Cell Line
|2 MeSH
650 _ 2 |a Dogs
|2 MeSH
650 _ 2 |a Lipid Bilayers: metabolism
|2 MeSH
650 _ 2 |a Phosphatidylinositols: metabolism
|2 MeSH
650 _ 2 |a Protein Binding
|2 MeSH
650 _ 2 |a Protein Conformation
|2 MeSH
650 _ 2 |a Protein Multimerization
|2 MeSH
650 _ 2 |a Solutions
|2 MeSH
650 _ 2 |a trans-Golgi Network
|2 MeSH
693 _ _ |0 EXP:(DE-H253)Unknown-BL-20150101
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|x 0
|6 EXP:(DE-H253)Unknown-BL-20150101
700 1 _ |a Coskun, Ü.
700 1 _ |a Rössle, M.
700 1 _ |a Buschhorn, S. B.
700 1 _ |a Grzybek, M.
700 1 _ |a Dafforn, T. R.
700 1 _ |a Lenoir, M.
700 1 _ |a Overduin, M.
700 1 _ |a Simons, K.
773 _ _ |a 10.1073/pnas.0911789106
|g Vol. 106, p. 21121-21125
|0 PERI:(DE-600)1461794-8
|q 106<21121-21125
|p 21121-21125
|t Proceedings of the National Academy of Sciences of the United States of America
|v 106
|y 2009
|x 1091-6490
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2795549
856 4 _ |u https://bib-pubdb1.desy.de/record/94235/files/Cao_et_al_PNAS_09-for%20DESY.zip
|y OpenAccess
909 C O |o oai:bib-pubdb1.desy.de:94235
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910 1 _ |0 I:(DE-HGF)0
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913 1 _ |0 G:(DE-HGF)POF1-540
|v Kondensierte Materie
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|b Struktur der Materie
|l Großgeräte für die Forschung mit Photonen, Neutronen, Ionen
914 1 _ |a (c) National Academy of Sciences.
|y 2009
915 _ _ |a JCR/ISI refereed
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920 _ 1 |i European Molecular Biology Laboratory
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920 1 _ |0 I:(DE-H253)EMBL_-2012_-20130307
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